BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 25359

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25359

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Title: BamA barrel in nanodiscs   PubMed: 25638436

Deposition date: 2014-11-20 Original release date: 2015-02-06

Authors: Morgado, Leonor; Hiller, Sebastian

Citation: Morgado, Leonor; Zeth, Kornelius; Burmann, Bjoern; Maier, Timm; Hiller, Sebastian. "Characterization of the insertase BamA in three different membrane mimetics by solution NMR spectroscopy"  J. Biomol. NMR 61, 333-345 (2015).

Assembly members:
BamA, polymer, 411 residues, Formula weight is not available

Natural source:   Common Name: Escherichia coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
BamA: MGSSHHHHHHSSGENLYFQH MRNTGSFNFGIGYGTESGVS FQAGVQQDNWLGTGYAVGIN GTKNDYQTYAELSVTNPYFT VDGVSLGGRLFYNDFQADDA DLSDYTNKSYGTDVTLGFPI NEYNSLRAGLGYVHNSLSNM QPQVAMWRYLYSMGEHPSTS DQDNSFKTDDFTFNYGWTYN KLDRGYFPTDGSRVNLTGKV TIPGSDNEYYKVTLDTATYV PIDDDHKWVVLGRTRWGYGD GLGGKEMPFYENFYAGGSST VRGFQSNTIGPKAVYFPHQA SNYDPDYDYESATQDGAKDL SKSDDAVGGNAMAVASLEFI TPTPFISDKYANSVRTSFFW DMGTVWDTNWDSSQYSGYPD YSDPSNIRMSAGIALQWMSP LGPLVFSYAQPFKKYDGDKA EQFQFNIGKTW

Data sets:
Data typeCount
13C chemical shifts41
15N chemical shifts20
1H chemical shifts20

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1BamA transmembrane domain1

Entities:

Entity 1, BamA transmembrane domain 411 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYGLUASNLEUTYRPHEGLNHIS
3   METARGASNTHRGLYSERPHEASNPHEGLY
4   ILEGLYTYRGLYTHRGLUSERGLYVALSER
5   PHEGLNALAGLYVALGLNGLNASPASNTRP
6   LEUGLYTHRGLYTYRALAVALGLYILEASN
7   GLYTHRLYSASNASPTYRGLNTHRTYRALA
8   GLULEUSERVALTHRASNPROTYRPHETHR
9   VALASPGLYVALSERLEUGLYGLYARGLEU
10   PHETYRASNASPPHEGLNALAASPASPALA
11   ASPLEUSERASPTYRTHRASNLYSSERTYR
12   GLYTHRASPVALTHRLEUGLYPHEPROILE
13   ASNGLUTYRASNSERLEUARGALAGLYLEU
14   GLYTYRVALHISASNSERLEUSERASNMET
15   GLNPROGLNVALALAMETTRPARGTYRLEU
16   TYRSERMETGLYGLUHISPROSERTHRSER
17   ASPGLNASPASNSERPHELYSTHRASPASP
18   PHETHRPHEASNTYRGLYTRPTHRTYRASN
19   LYSLEUASPARGGLYTYRPHEPROTHRASP
20   GLYSERARGVALASNLEUTHRGLYLYSVAL
21   THRILEPROGLYSERASPASNGLUTYRTYR
22   LYSVALTHRLEUASPTHRALATHRTYRVAL
23   PROILEASPASPASPHISLYSTRPVALVAL
24   LEUGLYARGTHRARGTRPGLYTYRGLYASP
25   GLYLEUGLYGLYLYSGLUMETPROPHETYR
26   GLUASNPHETYRALAGLYGLYSERSERTHR
27   VALARGGLYPHEGLNSERASNTHRILEGLY
28   PROLYSALAVALTYRPHEPROHISGLNALA
29   SERASNTYRASPPROASPTYRASPTYRGLU
30   SERALATHRGLNASPGLYALALYSASPLEU
31   SERLYSSERASPASPALAVALGLYGLYASN
32   ALAMETALAVALALASERLEUGLUPHEILE
33   THRPROTHRPROPHEILESERASPLYSTYR
34   ALAASNSERVALARGTHRSERPHEPHETRP
35   ASPMETGLYTHRVALTRPASPTHRASNTRP
36   ASPSERSERGLNTYRSERGLYTYRPROASP
37   TYRSERASPPROSERASNILEARGMETSER
38   ALAGLYILEALALEUGLNTRPMETSERPRO
39   LEUGLYPROLEUVALPHESERTYRALAGLN
40   PROPHELYSLYSTYRASPGLYASPLYSALA
41   GLUGLNPHEGLNPHEASNILEGLYLYSTHR
42   TRP

Samples:

BamA_nanodiscs: BamA, [U-13C; U-15N; U-2H], 850 uM; MES 25 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 0.17 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCBamA_nanodiscsisotropicsample_conditions_1
3D HNCACBBamA_nanodiscsisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

PROSA, Guntert - processing

CARA, Bartels et al. - processing

NMR spectrometers:

  • Bruker Ascend 700 MHz

Related Database Links:

PDB
DBJ BAA77852 BAB33602 BAG75700 BAI23538 BAI29053
EMBL CAP74746 CAQ30691 CAQ97064 CAR01552 CAR06402
GB AAB08606 AAC73288 AAD23568 AAG54479 AAK64508
REF NP_308206 NP_414719 NP_706122 WP_001240878 WP_001240879
SP A1A7M1 A7ZHR7 A7ZWC3 B1IQG4 B1XD46

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts